Binding studies of [H]Lyngbyatoxin A and [H]debromoaplysiatoxin to the phorbol ester receptor in a mouse epidermal particulate fraction

Abstract
The preparation of [H]lyngbyatoxin A by catalytic triton-proton exchange of lyngbyatoxin A and [H]debromoaplysia-toxin by tritiation - debromination of aplysiatoxin is described. The dose-response curves for the binding of [H]lyng-byatoxin A and [H]debromoaplysiatoxin to a mouse epidermal particulate fraction are virtually the same as the one previously described for [H]12-O-tetradecanoylphorbol-13-acetate ([HTPA). The specific binding of [HTPA, [H]-lyngbyatoxin A and [H]debromoaplysiatoxin to the mouse epidermal particulate fraction is inhibited to the same degree by unlabeled TPA, teleocidin, lyngbyatoxin A, aplysiatoxin and debromoaplysiatoxin. This study indicates that TPA, lyngbyatoxin A and debromoaplysiatoxin bind to the same high affinity receptor in mouse skin.